GLTP_ECOLI
ID GLTP_ECOLI Reviewed; 437 AA.
AC P21345; Q2M6M7;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Proton/glutamate-aspartate symporter {ECO:0000255|HAMAP-Rule:MF_02063, ECO:0000305};
DE AltName: Full=Glutamate-aspartate carrier protein {ECO:0000305};
DE AltName: Full=Proton-glutamate-aspartate transport protein {ECO:0000303|PubMed:1551855};
GN Name=gltP {ECO:0000255|HAMAP-Rule:MF_02063, ECO:0000303|PubMed:1971622,
GN ECO:0000303|PubMed:2537813}; OrderedLocusNames=b4077, JW4038;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ACTIVITY REGULATION, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=K12;
RX PubMed=1971622; DOI=10.1128/jb.172.6.3214-3220.1990;
RA Wallace B., Yang Y.-J., Hong J., Lum D.;
RT "Cloning and sequencing of a gene encoding a glutamate and aspartate
RT carrier of Escherichia coli K-12.";
RL J. Bacteriol. 172:3214-3220(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
RC STRAIN=K12;
RX PubMed=1551855; DOI=10.1128/jb.174.7.2391-2393.1992;
RA Tolner B., Poolman B., Wallace B., Konings W.N.;
RT "Revised nucleotide sequence of the gltP gene, which encodes the proton-
RT glutamate-aspartate transport protein of Escherichia coli K-12.";
RL J. Bacteriol. 174:2391-2393(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP FUNCTION, AND ACTIVITY REGULATION.
RC STRAIN=D2W;
RX PubMed=336628; DOI=10.1016/s0021-9258(17)38344-8;
RA Schellenberg G.D., Furlong C.E.;
RT "Resolution of the multiplicity of the glutamate and aspartate transport
RT systems of Escherichia coli.";
RL J. Biol. Chem. 252:9055-9064(1977).
RN [7]
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=B;
RX PubMed=2537813; DOI=10.1128/jb.171.3.1314-1319.1989;
RA Deguchi Y., Yamato I., Anraku Y.;
RT "Molecular cloning of gltS and gltP, which encode glutamate carriers of
RT Escherichia coli B.";
RL J. Bacteriol. 171:1314-1319(1989).
RN [8]
RP FUNCTION.
RX PubMed=8596452; DOI=10.1111/j.1365-2958.1995.mmi_18010123.x;
RA Tolner B., Ubbink-Kok T., Poolman B., Konings W.N.;
RT "Cation-selectivity of the L-glutamate transporters of Escherichia coli,
RT Bacillus stearothermophilus and Bacillus caldotenax: dependence on the
RT environment in which the proteins are expressed.";
RL Mol. Microbiol. 18:123-133(1995).
RN [9]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
CC -!- FUNCTION: Catalyzes the proton-dependent, binding-protein-independent
CC transport of glutamate and aspartate. {ECO:0000269|PubMed:1971622,
CC ECO:0000269|PubMed:2537813, ECO:0000269|PubMed:336628,
CC ECO:0000269|PubMed:8596452}.
CC -!- ACTIVITY REGULATION: Glutamate uptake is inhibited by L-cysteate and
CC beta-hydroxyaspartate. Inhibited by the uncoupler carbonylcyanide m-
CC chlorophenylhydrazone (CCCP). {ECO:0000269|PubMed:1971622,
CC ECO:0000269|PubMed:2537813, ECO:0000269|PubMed:336628}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=2.6 nmol/min/mg enzyme with glutamate as substrate
CC {ECO:0000269|PubMed:2537813};
CC Vmax=2.3 nmol/min/mg enzyme with aspartate as substrate
CC {ECO:0000269|PubMed:2537813};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_02063, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:1971622,
CC ECO:0000269|PubMed:2537813}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_02063}.
CC -!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter
CC (DAACS) (TC 2.A.23) family. GltP subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_02063, ECO:0000305}.
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DR EMBL; M32488; AAA23832.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M84805; AAA24323.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43171.1; -; Genomic_DNA.
DR EMBL; U00096; AAD13460.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78079.1; -; Genomic_DNA.
DR PIR; A42384; A42384.
DR RefSeq; NP_418501.1; NC_000913.3.
DR RefSeq; WP_000789592.1; NZ_LN832404.1.
DR AlphaFoldDB; P21345; -.
DR SMR; P21345; -.
DR BioGRID; 4262679; 10.
DR STRING; 511145.b4077; -.
DR TCDB; 2.A.23.1.1; the dicarboxylate/amino acid:cation (na(+) or h(+)) symporter (daacs) family.
DR PaxDb; P21345; -.
DR PRIDE; P21345; -.
DR EnsemblBacteria; AAD13460; AAD13460; b4077.
DR EnsemblBacteria; BAE78079; BAE78079; BAE78079.
DR GeneID; 948591; -.
DR KEGG; ecj:JW4038; -.
DR KEGG; eco:b4077; -.
DR PATRIC; fig|1411691.4.peg.2626; -.
DR EchoBASE; EB0400; -.
DR eggNOG; COG1301; Bacteria.
DR HOGENOM; CLU_019375_7_0_6; -.
DR InParanoid; P21345; -.
DR OMA; ICSFVVP; -.
DR PhylomeDB; P21345; -.
DR BioCyc; EcoCyc:GLTP-MON; -.
DR BioCyc; MetaCyc:GLTP-MON; -.
DR PRO; PR:P21345; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005280; F:amino acid:proton symporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006835; P:dicarboxylic acid transport; IMP:EcoCyc.
DR Gene3D; 1.10.3860.10; -; 1.
DR HAMAP; MF_02063; GltP_subfam; 1.
DR InterPro; IPR034703; GltP.
DR InterPro; IPR001991; Na-dicarboxylate_symporter.
DR InterPro; IPR018107; Na-dicarboxylate_symporter_CS.
DR InterPro; IPR036458; Na:dicarbo_symporter_sf.
DR PANTHER; PTHR42865; PTHR42865; 1.
DR Pfam; PF00375; SDF; 1.
DR SUPFAM; SSF118215; SSF118215; 1.
DR PROSITE; PS00713; NA_DICARBOXYL_SYMP_1; 1.
DR PROSITE; PS00714; NA_DICARBOXYL_SYMP_2; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..437
FT /note="Proton/glutamate-aspartate symporter"
FT /id="PRO_0000202088"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..50
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 72..84
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 106..159
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..210
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 254..292
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..324
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 346..361
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 383..387
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 409..437
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
SQ SEQUENCE 437 AA; 47159 MW; 62E1A5FC16EA54BE CRC64;
MKNIKFSLAW QILFAMVLGI LLGSYLHYHS DSRDWLVVNL LSPAGDIFIH LIKMIVVPIV
ISTLVVGIAG VGDAKQLGRI GAKTIIYFEV ITTVAIILGI TLANVFQPGA GVDMSQLATV
DISKYQSTTE AVQSSSHGIM GTILSLVPTN IVASMAKGEM LPIIFFSVLF GLGLSSLPAT
HREPLVTVFR SISETMFKVT HMVMRYAPVG VFALIAVTVA NFGFSSLWPL AKLVLLVHFA
ILFFALVVLG IVARLCGLSV WILIRILKDE LILAYSTASS ESVLPRIIEK MEAYGAPVSI
TSFVVPTGYS FNLDGSTLYQ SIAAIFIAQL YGIDLSIWQE IILVLTLMVT SKGIAGVPGV
SFVVLLATLG SVGIPLEGLA FIAGVDRILD MARTALNVVG NALAVLVIAK WEHKFDRKKA
LAYEREVLGK FDKTADQ
